4f0m

From Proteopedia

(Difference between revisions)

Revision as of 02:47, 11 December 2016

UNACTIVATED RUBISCO with MAGNESIUM AND A WATER MOLECULE BOUND

Structural highlights

4f0m is a 2 chain structure with sequence from Galdieria sulphuraria. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Related:	4f0h, 4f0k
Activity:	Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RBL_GALSU] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] [RBS_GALSU] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site (By similarity).

Publication Abstract from PubMed

Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is a crucial enzyme in carbon fixation and the most abundant protein on earth. It has been studied extensively by biochemical and structural methods; however, the most essential activation step has not yet been described. Here, we describe the mechanistic details of Lys carbamylation that leads to RuBisCO activation by atmospheric CO(2). We report two crystal structures of nitrosylated RuBisCO from the red algae Galdieria sulphuraria with O(2) and CO(2) bound at the active site. G. sulphuraria RuBisCO is inhibited by cysteine nitrosylation that results in trapping of these gaseous ligands. The structure with CO(2) defines an elusive, preactivation complex that contains a metal cation Mg(2+) surrounded by three H(2)O/OH molecules. Both structures suggest the mechanism for discriminating gaseous ligands by their quadrupole electric moments. We describe conformational changes that allow for intermittent binding of the metal ion required for activation. On the basis of these structures we propose the individual steps of the activation mechanism. Knowledge of all these elements is indispensable for engineering RuBisCO into a more efficient enzyme for crop enhancement or as a remedy to global warming.

Structural mechanism of RuBisCO activation by carbamylation of the active site lysine.,Stec B Proc Natl Acad Sci U S A. 2012 Oct 29. PMID:23112176^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Stec B. Structural mechanism of RuBisCO activation by carbamylation of the active site lysine. Proc Natl Acad Sci U S A. 2012 Oct 29. PMID:23112176 doi:http://dx.doi.org/10.1073/pnas.1210754109

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4f0m"

@@ Line 1: / Line 1: @@
 ==UNACTIVATED RUBISCO with MAGNESIUM AND A WATER MOLECULE BOUND==
 <StructureSection load='4f0m' size='340' side='right' caption='[[4f0m]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f0h|4f0h]], [[4f0k|4f0k]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f0m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f0m RCSB], [http://www.ebi.ac.uk/pdbsum/4f0m PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f0m OCA], [http://pdbe.org/4f0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f0m RCSB], [http://www.ebi.ac.uk/pdbsum/4f0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f0m ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/RBL_GALSU RBL_GALSU]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] [[http://www.uniprot.org/uniprot/RBS_GALSU RBS_GALSU]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4f0m" style="background-color:#fffaf0;"></div>
 ==See Also==

4f0m

From Proteopedia

Revision as of 02:47, 11 December 2016

UNACTIVATED RUBISCO with MAGNESIUM AND A WATER MOLECULE BOUND

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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